This article is an overview about the functions of enzymes in the body and their use as convenient targets for pharmacological drugs.

Steps

1

Learn what are enzymes and how they are synthesized in the body. Enzymes are a class of proteins that have special functions in the body of living organisms including human individuals. These enzymes are synthesized in the body by the same mechanism of proteins translational processes that involves the coding of amino acids by codons that are comprised each of three DNA bases. Each codon of three neighboring DNA bases codes for one amino acid. This amino acid is in turn transported to the cellular ribosome using special type of RNA molecule that is called transfer RNA molecule. These amino acids that are collected at the ribosomal surface become covalently attached to each other by the effect of specialized enzymes. Eventually the formed protein leaves the ribosomal surface and becomes an active protein that can serve one of several functions in the body including enzymatic functions.

2

Study the differences between enzymes and other forms of proteins. Enzymes differ than other forms of proteins by their special morphological chemical structure that contains an active site. This active site is located within a small hole in the structure of the tertiary folded protein. It is presumed that catalytic effects of all enzymes occur within these small holes of all proteins. These holes contain few amino acids that have immense physiological value due to their participation in performing the catalysis of the metabolic reactions. Enzymes usually have chiral structure that gives it character as a selective catalyst for the biochemical reactions inside the cells of body. Enzymatic catalysis inside the body usually proceeds at body temperature of 37 °C (99 °F). This is in contrast to chemical reactions that occur in the chemical laboratory which can require high temperature to proceed. Also typical of enzymatic reactions inside the body is the use of water as the medium for the reaction.

3

See the differences between metabolic reactions inside the body and chemical reactions in the chemistry laboratory. In the chemical laboratory this process usually occurs in organic solvents. Also inside the body there is no need for separation of biochemical products of the metabolism in the cells of the body. On the other hand there is a need to isolate the products of reactions that take place in the chemistry laboratory by evaporation technique of the organic solvent. Also enzymes mediated biochemical reactions are highly selective and specific in their progression. This is rarely observed in the chemistry laboratory with normal non biochemical reactions. These non metabolic reactions usually involve multiple products of the chemical reaction that poses difficulties of separating them. In this respect enzymes catalyzed reactions are superior to chemical reactions that take place in the chemistry laboratory.

4

Learn the importance of enzymes for the performance of metabolic reactions inside the body. All metabolic reactions inside all living organisms share the common characteristic of being performed under enzymatic catalytic conditions. Metabolic reactions cannot proceed without the assistance of enzymes. This is partly due to the limitation of low temperature on the reaction conditions inside the body. Enzymes are used pharmacologically in the treatment of various medical disorders. Pharmacologists use the fact the these biochemical reactions do not proceed without the assistance of the enzymes for designing pharmacological drugs in order to treat diseases in the body of humans. Especially notable here is the effect of these drugs on microbial agents such as bacterial microorganisms. These microorganisms use very specific metabolic pathways for their life sustaining. In this respect they use special enzymes to drive these metabolic reactions to completion. Pharmacological drugs are used in most cases to inhibit the function of key enzymes in the metabolic pathways of important biochemical reactions within the bacterial microorganism.

5

Study the role of enzyme inhibition in the treatment of medical disorders. Inhibition of these important enzymes can be either reversible or irreversible. Irreversible inhibition refers to the inability of the enzyme to restore its biological effect by chemical means. This is usually obtained by the binding of the inhibitor drug covalently to one of the amino acids in the active site of the enzyme. This usually neutralizes completely the catalytic function of the enzyme. On the other hand reversible inhibition can usually be modified to restore the full catalytic function of the enzyme. This is usually done by increasing the concentration of competitive substrate in the body to the pharmacologic drug. This can diminish the effect of the drug on the catalysis of the enzyme. Reversible inhibition is usually obtained by the formation of electrostatic interaction between the drug and the amino acid within the active site of the enzyme.

6

Learn about the types of interactions between pharmacological drugs and the active site of the enzyme. One type of such common interactions is the hydrogen bonding type of electrostatic interactions. The kinetics of enzymatic catalysis is a major concern of research that is done in order to elucidate the presumed catalytic function of the enzyme. Also structural studies of amino acids sequence of the enzymatic skeleton is less likely done due to the usual long sequence of amino acids that characterizes most enzymes in the body. Genetic diseases can affect the quality of the enzyme structure by virtue of the dependence of its synthesis on the sequence of the DNA bases that usually code for its synthesis. Also cancer can cause defective enzymes synthesis due to the defective genetic material that is triggered by the mutational effect of the cancer.